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Q4WC60 (BTGE_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable beta-glucosidase btgE

EC=3.2.1.21
Alternative name(s):
Beta-D-glucoside glucohydrolase btgE
Cellobiase btgE
Gentiobiase btgE
Gene names
Name:btgE
ORF Names:AFUA_8G05610
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length565 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Beta-glucosidases are one of a number of cellulolytic enzymes involved in the degradation of cellulosic biomass. Catalyzes the last step releasing glucose from the inhibitory cellobiose By similarity.

Catalytic activity

Hydrolysis of terminal, non-reducing beta-D-glucosyl residues with release of beta-D-glucose.

Pathway

Glycan metabolism; cellulose degradation.

Subcellular location

Secretedcell wall By similarity. Note: Covalently-linked to the cell wall By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 17 family.

Sequence caution

The sequence EAL85324.1 differs from that shown. Reason: Erroneous gene model prediction.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentCell wall
Secreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentcell wall

Inferred from electronic annotation. Source: UniProtKB-SubCell

extracellular region

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionbeta-glucosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 565547Probable beta-glucosidase btgE
PRO_0000395133

Regions

Compositional bias44 – 287244Thr-rich

Sites

Active site5011Nucleophile By similarity
Active site5551Proton donor By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4WC60 [UniParc].

Last modified June 15, 2010. Version 2.
Checksum: 4D06B871D8835ACC

FASTA56558,148
        10         20         30         40         50         60 
MRGAILATAA ALAGTAMADV AHMRRHGHDS FHQRRSPLAE ADATCGCTTE VVTVWGPPTL 

        70         80         90        100        110        120 
IPVASPTPST VTSEAVTTLH STSTTTVTVI ASASTPAASP SPATDKVPLP TPAITNFPST 

       130        140        150        160        170        180 
GVYTIPATTV TVFDTTTVCG ATTTELPAGT HTYGGVTTVV ETATTVVCPY ATVEPSGTTV 

       190        200        210        220        230        240 
TSVIKTTTYV CPSAGTYTIA PTTTTVPTST VIVYPTPAVI TPGTYTQPEQ TVTVTRTDYT 

       250        260        270        280        290        300 
YVCPFTGQDE PTSAPAAPST TAVPATTTAA PETTTAAPDT TTAVPSTSSA APSSSSTAPA 

       310        320        330        340        350        360 
STGAVSGQMG MTYTPYTKGG DCKDKSSVLS EVAALKSKGF THVRVYSTDC NSLEYIGEAA 

       370        380        390        400        410        420 
RTSGLQMIIG VFISSTGVSG AQDQVTAISK WAQWDLVSLI VVGNEAIQNG YCDASTLAGF 

       430        440        450        460        470        480 
ISSAKSAFQA AGYTGKVTTT EPINVWQAHG STLCGVCDIV GANIHPFFNA DVSADQAGKF 

       490        500        510        520        530        540 
VAQEIKVLES ICPGKDVLNL ETGWPHAGNA NGKAVPGTSE QAIAIKSIAD EVGSKSVFFS 

       550        560 
YFDDLWKEPG QFGVERYWGC FDTFN 

« Hide

References

[1]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AAHF01000013 Genomic DNA. Translation: EAL85324.1. Sequence problems.
RefSeqXP_747362.1. XM_742269.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5085.CADAFUAP00003231.

Proteomic databases

PRIDEQ4WC60.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUAT00003231; CADAFUAP00003231; CADAFUAG00003231.
GeneID3504706.
KEGGafm:AFUA_8G05610.

Phylogenomic databases

eggNOGCOG5309.
HOGENOMHOG000158427.
KOK01238.
OrthoDBEOG73FQWG.

Enzyme and pathway databases

UniPathwayUPA00696.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameBTGE_ASPFU
AccessionPrimary (citable) accession number: Q4WC60
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: June 15, 2010
Last modified: March 19, 2014
This is version 57 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries